Halogenated natural products possess diverse biological properties of pharmacological interest, including anti-fungal, anti-bacterial, anti-viral, and anti-inflammatory activities. The marine sediment-derived bacterium Streptomyces sp. CNQ-525, which produces a suite of chlorinated dihydroquinones, was used as a source for identifying novel halogenating enzymes.  Cloning and sequence analysis of the 43-kb napyradiomycin biosynthetic cluster (nap) yielded a diverse arrangement of biosynthetic genes involved in polyketide, terpenoid and halogenation biochemistry. The discovery of three vanadium chloroperoxidases (V-ClPOs) within this marine bacterial gene cluster was significant as these enzymes are quite rare in nature and have only been characterized in vitro from eukaryotic systems.  Through in vivo experiments, we have shown that the encoding genes are indeed functional as we were able to heterologously express the nap biosynthetic cluster in the surrogate host S. albus.  We propose that these V-ClPOs are responsible for the natural product chemistry associated with the napyradiomycin class of antibiotics involving chloronium-mediated terpenoid cyclization reations.  Our progress on the in vivo and in vitro functional characterization of the nap V-ClPOs will be presented, which points to their use as recombinant biocatalysts for the introduction of halogens to olefinic substrates in a regio- and stereo-controlled manner.